ID A0A4Q7JHZ0_METCM Unreviewed; 490 AA.
AC A0A4Q7JHZ0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU365081};
DE Short=PPIase {ECO:0000256|RuleBase:RU365081};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU365081};
GN ORFNames=I1G_00003924 {ECO:0000313|EMBL:RZR58906.1};
OS Pochonia chlamydosporia 123.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1052797 {ECO:0000313|EMBL:RZR58906.1};
RN [1] {ECO:0000313|EMBL:RZR58906.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=123 {ECO:0000313|EMBL:RZR58906.1};
RX PubMed=24530791; DOI=10.1016/j.fgb.2014.02.002;
RA Larriba E., Jaime M.D., Carbonell-Caballero J., Conesa A., Dopazo J.,
RA Nislow C., Martin-Nieto J., Lopez-Llorca L.V.;
RT "Sequencing and functional analysis of the genome of a nematode egg-
RT parasitic fungus, Pochonia chlamydosporia.";
RL Fungal Genet. Biol. 65:69-80(2014).
RN [2] {ECO:0000313|EMBL:RZR58906.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=123 {ECO:0000313|EMBL:RZR58906.1};
RA Studholme D.J.;
RT "Annotation of Pochonia chlamydospria.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|ARBA:ARBA00002388,
CC ECO:0000256|RuleBase:RU365081}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000971,
CC ECO:0000256|RuleBase:RU365081};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365081}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC subfamily. {ECO:0000256|ARBA:ARBA00010739,
CC ECO:0000256|RuleBase:RU365081}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RZR58906.1}.
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DR EMBL; AOSW02000925; RZR58906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q7JHZ0; -.
DR STRING; 1052797.A0A4Q7JHZ0; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd01921; cyclophilin_RRM; 1.
DR CDD; cd12235; RRM_PPIL4; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR035542; CRIP.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR035538; Cyclophilin_PPIL4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR45843; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR PANTHER; PTHR45843:SF1; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-LIKE 4; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365081};
KW Nucleus {ECO:0000256|RuleBase:RU365081};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU365081};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU365081}.
FT DOMAIN 6..172
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 251..329
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 176..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 55796 MW; 09CFA43E63F3B80F CRC64;
MSVLLETSVG DIVIDLLVEH APKLCENFLK LCKVKYYNFS PVHSVQKNFS FQTGDPLGPL
SKESDGGSSI WGHISADPAK RSFSAFFHPK LKHVERGTVS MATAPLSSDP ATRLAASQFI
ITLGEDTDFL DGKAAVFGKV VEGFDALEKI NEAIVDDKGY PLIDIRIKHT VILDDPYPDP
SGLREPSSSP PPTSEQLKTV RIADEAALHE DDGVDEAELE RRRRQNEANA QALTLEMMGD
LPFAEVKPPE NVLFVCKLNP VTGDEDLELI FGRFGKILSC EVIRDAKTGD SLQYAFIEYE
DKASCETAYF KMQGVLIDDR RIHVDFSQSV SKLSDVWRKD TNSKRRAHAS RGGWGGVEEL
EKRRQYRAEM DAPEKNNYGM VYGNEEMKGR HQLGGPTSRK GEDFSSREES RRKDHGSRSR
SPHRREEARD RQQWRRDVDY RGAGRDGDRR DRSYRSGDKD ENRPRERERD RDRHRDQGKY
HDRDNSYRRK
//
